Characterization of Two Endo-β-1,3-Glucanases from the Thermophilic Bacterium Fervidobacterium sp
5. Conclusions
Laminarinases are enzymes which could be applied in diverse fields, from biomass conversion, over yeast extract production, agents against fungal plant pathogens to the production of antiviral and antitumor therapeutics fromβ-1,3-glucans. The biochemical characterization of the two laminarinases FLamA and FLamB derived from aFervidobacteriumspecies revealed high specific activities and resistance to elevated temperatures and various additives which make both enzymes suitable candidates for application under harsh conditions. Moreover, the comparative analysis of both enzymes showed differences in their thermal stability and catalytic efficiency towardsβ-1,3-glucans, like laminarin and curdlan. In conclusion, these results will contribute to our knowledge of sequence-function correlations and will potentially help to improve activity and stability of laminarinases and other related glucanases.
Supplementary Materials:The following are available online athttp://www.mdpi.com/2073-4344/9/10/830/s1, Figure S1: Structural models of FLamA and FLamB, Figure S2: Amino acid alignment of the catalytic domains of FLamA and FLamB with other members of GH 16, Figure S3: Laminarinase activity of FLamA and FLamB after incubation at pH 3-11 and 4◦C for 24 h, Table S1: Purification of the recombinant FLamA and FLamB fromE. coli.
Author Contributions: C.B. designed the study and performed the experimental work. C.S., G.S. and G.A.
supervised this study. C.B. prepared the manuscript. C.S., J.C. and G.A. reviewed and edited the manuscript before submission.
Funding:This research was funded by BMBF (Bundesministerium für Bildung und Forschung, Germany) in the project LIPOMAR (Lipids and surfactants from marine biomass), FKZ 031A261.
Conflicts of Interest:The authors declare no conflict of interest.
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